PMID- 9111344
OWN - NLM
STAT- MEDLINE
DCOM- 19970515
LR  - 20210526
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 17
IP  - 5
DP  - 1997 May
TI  - GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of 
      steroid, thyroid, retinoid, and vitamin D receptors.
PG  - 2735-44
AB  - After binding to enhancer elements, transcription factors require transcriptional 
      coactivator proteins to mediate their stimulation of transcription initiation. A 
      search for possible coactivators for steroid hormone receptors resulted in 
      identification of glucocorticoid receptor interacting protein 1 (GRIP1). The 
      complete coding sequence for GRIP1, isolated from a mouse brain cDNA library, 
      contains an open reading frame of 1,462 codons. GRIP1 is the probable ortholog of 
      the subsequently identified human protein transcription intermediary factor 2 
      (TIF2) and is also partially homologous to steroid receptor coactivator 1 
      (SRC-1). The full-length GRIP1 interacted with the hormone binding domains (HBDs) 
      of all five steroid receptors in a hormone-dependent manner and also with HBDs of 
      class II nuclear receptors, including thyroid receptor alpha, vitamin D receptor, 
      retinoic acid receptor alpha, and retinoid X receptor alpha. In contrast to 
      agonists, glucocorticoid antagonists did not promote interaction between the 
      glucocorticoid receptor and GRIP1. In yeast cells, GRIP1 dramatically enhanced 
      the transcriptional activation function of proteins containing the HBDs of any of 
      the above-named receptors fused to the GAL4 DNA binding domain and thus served as 
      a transcriptional coactivator for them. This finding contrasts with previous 
      reports of TIF2 and SRC-1, which in mammalian cells enhanced the transactivation 
      activities of only a subset of the steroid and nuclear receptors that they 
      physically interacted with. GRIP1 also enhanced the hormone-dependent 
      transactivation activity of intact glucocorticoid receptor, estrogen receptor, 
      and mineralocorticoid receptor. Experiments with glucocorticoid receptor 
      truncation and point mutants indicated that GRIP1 interacted with and enhanced 
      the activity of the C-terminal AF-2 but not the N-terminal AF-1 transactivation 
      domain of the glucocorticoid receptor. These results demonstrate directly that 
      AF-1 and AF-2 domains accomplish their transactivation activities through 
      different mechanisms: AF-2 requires GRIP1 as a coactivator, but AF-1 does not.
FAU - Hong, H
AU  - Hong H
AD  - Department of Pathology, University of Southern California, Los Angeles 90033, 
      USA.
FAU - Kohli, K
AU  - Kohli K
FAU - Garabedian, M J
AU  - Garabedian MJ
FAU - Stallcup, M R
AU  - Stallcup MR
LA  - eng
SI  - GENBANK/U39060
GR  - DK43093/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Biomarkers)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (GAL4 protein, S cerevisiae)
RN  - 0 (IFNGR2 protein, human)
RN  - 0 (Ifngr2 protein, mouse)
RN  - 0 (NCOA2 protein, human)
RN  - 0 (Ncoa2 protein, mouse)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Nuclear Receptor Coactivator 2)
RN  - 0 (Receptors, Calcitriol)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Interferon)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Steroid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factors)
RN  - EC 2.3.1.48 (Histone Acetyltransferases)
RN  - EC 2.3.1.48 (NCOA1 protein, human)
RN  - EC 2.3.1.48 (Ncoa1 protein, mouse)
RN  - EC 2.3.1.48 (Nuclear Receptor Coactivator 1)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Biomarkers
MH  - DNA-Binding Proteins
MH  - Fungal Proteins/metabolism
MH  - Histone Acetyltransferases
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/genetics/*metabolism
MH  - Nuclear Receptor Coactivator 1
MH  - Nuclear Receptor Coactivator 2
MH  - Point Mutation
MH  - Receptors, Calcitriol/genetics
MH  - Receptors, Cytoplasmic and Nuclear/*genetics
MH  - Receptors, Interferon/genetics/metabolism
MH  - Receptors, Retinoic Acid/genetics
MH  - Receptors, Steroid/genetics
MH  - Receptors, Thyroid Hormone/genetics
MH  - Recombinant Fusion Proteins/metabolism
MH  - *Saccharomyces cerevisiae Proteins
MH  - Trans-Activators/genetics/*metabolism
MH  - Transcription Factors/chemistry/*metabolism
PMC - PMC232124
EDAT- 1997/05/01 00:00
MHDA- 1997/05/01 00:01
PMCR- 1997/05/01
CRDT- 1997/05/01 00:00
PHST- 1997/05/01 00:00 [pubmed]
PHST- 1997/05/01 00:01 [medline]
PHST- 1997/05/01 00:00 [entrez]
PHST- 1997/05/01 00:00 [pmc-release]
AID - 10.1128/MCB.17.5.2735 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1997 May;17(5):2735-44. doi: 10.1128/MCB.17.5.2735.